Toniolo, C and Crisma, M and Valle, G and Bonora, GM and Polinelli, S and Becker, EL and Freer, RJ (1989) Conformationally restricted formyl methionyl tripeptide chemoattractants: a three-dimensional structure-activity study of analogs incorporating a C alpha,alpha-dialkylated glycine at position 2. In: Pept Res, 2 (4). pp. 275-281.
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Abstract
The conformationally restricted CHO-L-Met-Xxx-L-Phe-OY (where Xxx = Aib, Ac3c, Ac5c, Ac6c, and Ac7c; Y = H, Me) tripeptides, analogs of the chemoattractant CHO-L-Met-L-Leu-L-Phe-OH, have been synthesized in solution by classical methods and fully characterized. Compounds were compared to determine the combined effect of backbone conformational preferences and side-chain bulkiness on the relation of three-dimensional structure to biological activity. Each peptide was tested for its ability to induce granule enzyme secretion from rabbit peritoneal polymorphonuclear leukocytes. In parallel, a conformational analysis on the CHO-blocked peptide and their tertbutyloxycarbonylated synthetic precursors was performed in the crystal state and in solution using X-ray diffraction, infrared absorption, and 1H nuclear magnetic resonance. The biological and conformational data are discussed in relation to the proposed model of the chemotactic peptide receptor of rabbit neutrophils.
| Item Type: | Journal Article |
|---|---|
| Publication: | Pept Res |
| Publisher: | National Center for Biotechnology Information |
| Additional Information: | Copyright of this article belongs to National Center for Biotechnology Information. |
| Department/Centre: | Division of Biological Sciences > Molecular Biophysics Unit |
| Date Deposited: | 20 May 2010 06:36 |
| Last Modified: | 19 Sep 2010 06:00 |
| URI: | http://eprints.iisc.ac.in/id/eprint/27236 |
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